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Antimicrobial and Enzyme Activity of Endophytic Fungi Isolated from Tulsi

JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL SCIENCES 03/2012; 16(16):1-6.

ABSTRACT A study was carried out to isolate endophytic fungi from Ocimum species (Tulsi) and to assess their antimicrobial activity against Pseudomonas aeroginosa, Mycobacterium smegmatis, Salmonella typhimurium, Candida albicans and Penicillium chrysogenum and production of enzymes such as amylase, protease and tyrosinase. In this study forty endophytic fungi were isolated from leaves and branches of Tulsi. Out of forty endophytic fungal isolates, six isolates showed the inhibition activity against test microorganisms done by dual culture method. The isolate P14T1 exhibited a high antimicrobial activity against Candida albicans (22mm). The crude extract of P13T5 isolate showed highest zone of inhibition against Pseudomonas aeroginosa (21mm) by well and disc diffusion method. 50% of fungal isolates found positive for amylase and protease enzymes production and 27.5% showed positive for tyrosinase. The results of the study suggest that endophytic fungi associated with Tulsi are potential agents for antimicrobial activity and production of enzyme.

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    ABSTRACT: Five different endophytic fungi was isolated and identified from the various parts of Viscum album, protein isolated from the endophytic fungi Alternaria sp and Viscum album was identified as lectin based on haemagglutination assay, isolated lectin was blood group specific lectin agglutinating A+ve erythrocytes. SDSPAGE showed the molecular weight of 64 kDa protein was observed in endophytic Alternaria sp similar to Viscum album, PAS staining of NATIVE PAGE confirms the presence of lectin, MALDI-TOF-MS analysis of endophytic fungal lectin and MASCOT peptide mass finger printing reported that endophytic fungal lectin belongs to antiviral protein and ribosome inactivating protein family, observed peptide sequence K.NGALPKPLELK, identified as a conserved sequence pattern in the ribosome inactivating protein (RIPL1_PHYDI) of Phytolacca dioica (Bella sombra) tree and antiviral protein(RIPS_PHYAM) of Phytolacca americana (American pokeweed), this confirms that endophytic fungi Alternaria sp capable of producing lectin having antiviral and anticancer activity. Endophytic fungal lectin showed in vitro antibacterial activity on human pathogenic bacteria, maximum inhibition of 9 mm in Pseudomonas sp, 11 mm inhibition in Salmonella sp was observed from endophytic lectin extract.
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    ABSTRACT: Five different endophytic fungi was isolated and identified from the various parts of Viscum album, protein isolated from the endophytic fungi Alternaria sp and Viscum album was identified as lectin based on haemagglutination assay, isolated lectin was blood group specific lectin agglutinating A+ve erythrocytes. SDSPAGE showed the molecular weight of 64 kDa protein was observed in endophytic Alternaria sp similar to Viscum album, PAS staining of NATIVE PAGE confirms the presence of lectin, MALDI-TOF-MS analysis of endophytic fungal lectin and MASCOT peptide mass finger printing reported that endophytic fungal lectin belongs to antiviral protein and ribosome inactivat-ing protein family, observed peptide sequence K.NGALPKPLELK, identified as a conserved sequence pattern in the ribosome inactivating protein (RIPL1_PHYDI) of Phytolacca dioica (Bella sombra) tree and antiviral protein(RIPS_PHYAM) of Phytolacca americana (American pokeweed), this confirms that endophytic fungi Alternaria sp capable of producing lectin having antiviral and anticancer activity. Endo-phytic fungal lectin showed in vitro antibacterial activity on human pathogenic bacteria, maximum inhibition of 9 mm in Pseudomonas sp, 11 mm inhibition in Salmonella sp was observed from endophytic lectin extract. Viscum album L. is a common epiphytic parasite plant of the family Loranthaceae. The plant is widely distributed in tropical and sub-tropical Africa, Asia and Europe 4 . The modern phytochemical research showed that V. album is the rich source of active compounds. Viscum album aqueous extracts used were as a complementary medicine in cancer therapy. Various clinical studies have shown that Viscum album preparations improve the quality of life in different cancer patients. Biologically active components of V.album extracts include Mistletoe Lectins (ML), viscotoxins, polyphenols and polysaccha-rides 5 . The treatment with purified ML from Viscum album preparations has been shown to be associated with tumor regression in several in vivo experimental models of tumoral implantation. European Mistletoe lectins have been classified in to three lectins. VAA-I shows specific-ity to D-galactose and N –acetylgalactosamine. The VAA-I are type-2 ribosome inactivating proteins composed of two different subunits, an A-and B-chain linked by disulfide-bridge. The A-chain is capable of inactivating the 60S ribosomal subunit of eukaryotic cells resulting in inhibition of protein synthesis. The B-chain is capable of binding to cell surface glycoconjugates and thereby permits entry into the cell 6 . Lectin II is a D-galactose and N-acetylgalactosamine and lectin 1. INTRODUCTION: Lectins are carbohydrate binding proteins which bind to glycopro-teins, glycolipids and also polysaccharides 1 , which mediate various kind of biological processes by binding to different sugar moiety 2 . Lectins has the ability to recognize and bind reversibly to specific carbohydrate ligands without any chemical modification that distin-guish lectins from other carbohydrate binding proteins, because of it makes them invaluable tools in biomedical and glycoconjugate re-search. An important characteristic property of lectins is their ability to agglutinate erythrocytes in vitro. That is why, they frequently called agglutinins. Lectins from different source inhibit cancer cells growth, they are able to induce apoptosis and activate the immune system by stimulating the proliferation of T-lymphocytes. Lectins are found in all kinds of organism including animals, plants, fungi, bacteria and viruses 3 .

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